The Active Sites of the Native Cytochrome-c Oxidase from Bovine Heart Mitochondria: EXAFS-Spectroscopic Characterization of a Novel Homobinuclear Copper Center(CuA) and of the Heterobinuclear Fea3-CuB Center

1995 ◽  
Vol 34 (1314) ◽  
pp. 1488-1492 ◽  
Author(s):  
Gerald Henkel ◽  
Arnd Müller ◽  
Stefan Weissgräber ◽  
Gerhard Buse ◽  
Tewfik Soulimane ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Active Sites ◽  
Spectroscopic Characterization ◽  
Heart Mitochondria ◽  
Bovine Heart ◽  
Copper Center

scholarly journals Proton-transfer pathways in the mitochondrial S. cerevisiae cytochrome c oxidase

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Markus L. Björck ◽  
Jóhanna Vilhjálmsdóttir ◽  
Andrew M. Hartley ◽  
Brigitte Meunier ◽  
Linda Näsvik Öjemyr ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Proton Transfer ◽  
Cytochrome C Oxidase ◽  
Proton Pumping ◽  
Heart Mitochondria ◽  
Negative Side ◽  
Bovine Heart ◽  
Proton Uptake ◽  
Mammalian Counterpart ◽  
Kinetics Of

AbstractIn cytochrome c oxidase (CytcO) reduction of O2 to water is linked to uptake of eight protons from the negative side of the membrane: four are substrate protons used to form water and four are pumped across the membrane. In bacterial oxidases, the substrate protons are taken up through the K and the D proton pathways, while the pumped protons are transferred through the D pathway. On the basis of studies with CytcO isolated from bovine heart mitochondria, it was suggested that in mitochondrial CytcOs the pumped protons are transferred though a third proton pathway, the H pathway, rather than through the D pathway. Here, we studied these reactions in S. cerevisiae CytcO, which serves as a model of the mammalian counterpart. We analyzed the effect of mutations in the D (Asn99Asp and Ile67Asn) and H pathways (Ser382Ala and Ser458Ala) and investigated the kinetics of electron and proton transfer during the reaction of the reduced CytcO with O2. No effects were observed with the H pathway variants while in the D pathway variants the functional effects were similar to those observed with the R. sphaeroides CytcO. The data indicate that the S. cerevisiae CytcO uses the D pathway for proton uptake and presumably also for proton pumping.

scholarly journals 2P092 Structure of active sites of oxidized bovine heart cytochrome c oxidase

2004 ◽  
Vol 44 (supplement) ◽  
pp. S132
Author(s):  
H. Aoyama ◽  
K. Muramoto ◽  
M. Suga ◽  
K. Hirata ◽  
E. Yamashita ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Active Sites ◽  
Bovine Heart
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